UniProt ID | MIPT3_MOUSE | |
---|---|---|
UniProt AC | Q149C2 | |
Protein Name | TRAF3-interacting protein 1 | |
Gene Name | Traf3ip1 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 625 | |
Subcellular Localization | Cytoplasm, cytoskeleton . Cell projection, cilium . Cytoplasm, cytoskeleton, cilium axoneme . Cytoplasm, cytoskeleton, cilium basal body . Microtubules. In the cilium, it is observed at the ciliary base, ciliary transition zone and ciliary tip. | |
Protein Description | Plays an inhibitory role on IL13 signaling by binding to IL13RA1. Involved in suppression of IL13-induced STAT6 phosphorylation, transcriptional activity and DNA-binding. Recruits TRAF3 and DISC1 to the microtubules (By similarity). Involved in epithelial morphogenesis and in the regulation of microtubule cytoskeleton organization. Is a negative regulator of microtubule stability, acting through the control of MAP4 levels. [PubMed: 26487268 Involved in ciliogenesis] | |
Protein Sequence | MNAAVVRRTQEALGKVIRRPPLTEKLLNKPPFRYLHDIITEVIRITGFMKGLYTDAEMKSENVKDKDAKISFLQKAIDVVMMVSGEPLAAKPARIVAGHEPERTNELLQLIGKCCLSKLSSDEAVKRVLAGDKGDSRGRAQRTSKAQEPNNKSGKEEESRIHKEDKRSSEAKERSASAEHKQKEELKEDSKPREKERDKEKAKEADRDRHRDPDRDRNRDGEREKARARAKDRDRNNRDRDREAERDRERDRRSEGGKEKERVKDRDRDRDKGRDRERRKSKNGEHTRDPDREKSRDADKPEKKSSSSGEISRKLSDGSFKDVKAEMEADISVGASRSSTLKPSKRRSKHSLEGDSPSDAEVEAGPAGQDKPEVMENAEVPSELPSSLRRIPRPGSARPAPPRVKRQESTETLVVDRSGSGKTVSSVIIDSQNSDNEDDEQFVVEAAPQLSEIADIDMVPSGELEDEEKHGGLVKKILETKKDYEKLQQSLKPGEKERSLIFESAWKKEKDIVSKEIEKLRVSIQTLCKSALPLGKIMDYIQEDVDAMQNELQLWHSENRQHAEALSQEQSITDSAVEPLKAELSELEQQIRDQQDKICAVKANILKNEEKIQKMVHSINLSSRR | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
84 | Phosphorylation | IDVVMMVSGEPLAAK HCEEEECCCCCCCCC | 21.39 | 27357545 | |
118 | Acetylation | IGKCCLSKLSSDEAV HHHHHHHCCCCHHHH | 39.17 | 2390093 | |
126 | Acetylation | LSSDEAVKRVLAGDK CCCHHHHHHHHCCCC | 43.78 | 23576753 | |
133 | Acetylation | KRVLAGDKGDSRGRA HHHHCCCCCCHHHHH | 64.79 | 2390109 | |
136 | Phosphorylation | LAGDKGDSRGRAQRT HCCCCCCHHHHHHHC | 45.35 | 19854140 | |
190 | Phosphorylation | KEELKEDSKPREKER HHHHHHCCCHHHHHH | 45.72 | 28464351 | |
306 | Phosphorylation | DKPEKKSSSSGEISR CCCCCCCCCCCCHHH | 37.09 | 25338131 | |
316 | Phosphorylation | GEISRKLSDGSFKDV CCHHHHHCCCCHHHH | 42.85 | 26824392 | |
319 | Phosphorylation | SRKLSDGSFKDVKAE HHHHCCCCHHHHHHH | 33.83 | 22817900 | |
351 | Phosphorylation | SKRRSKHSLEGDSPS CCCCCCCCCCCCCCC | 31.67 | 25293948 | |
356 | Phosphorylation | KHSLEGDSPSDAEVE CCCCCCCCCCCCCCC | 36.84 | 21183079 | |
358 | Phosphorylation | SLEGDSPSDAEVEAG CCCCCCCCCCCCCCC | 54.10 | 28507225 | |
387 | Phosphorylation | VPSELPSSLRRIPRP CCCCCCHHHCCCCCC | 24.77 | 23140645 | |
409 | Phosphorylation | PRVKRQESTETLVVD CCCCCCCCCCEEEEC | 24.17 | 25521595 | |
410 | Phosphorylation | RVKRQESTETLVVDR CCCCCCCCCEEEECC | 32.03 | 27742792 | |
412 | Phosphorylation | KRQESTETLVVDRSG CCCCCCCEEEECCCC | 25.58 | 27742792 | |
614 | Acetylation | KNEEKIQKMVHSINL CCHHHHHHHHHHCCC | 46.49 | 7624015 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of MIPT3_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MIPT3_MOUSE !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of MIPT3_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of MIPT3_MOUSE !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409, AND MASSSPECTROMETRY. |